Evidence map›Paper›PMID 16051301›Full record

ArticleVirology2005

Mutagenesis of the murine hepatitis virus nsp1-coding region identifies residues important for protein processing, viral RNA synthesis, and viral replication.

Sarah M Brockway, Mark R Denison

Abstract read
In one paragraph

Article in Virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

53 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Structure of nonstructural protein 1 from SARS-CoV-2.bioRxiv : the preprint server for biology · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. Coronavirus cis-Acting RNA Elements.Advances in virus research · 2016
    Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Sarah M BrockwayDepartment of Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
Mark R Denison

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI Jin Chen · 1995 to 2026
$172.8M
TRAINING GRANT IN MECHANISMS OF VASCULAR DISEASET32HL007751 · NHLBI · VANDERBILT UNIVERSITY · PI BOCK, PAUL E · 1994 to 2014
$6.6M
POLYMERASE PROTEINS IN CORONAVIRUS REPLICATIONR01AI026603 · NIAID · VANDERBILT UNIVERSITY MEDICAL CENTER · PI DENISON, MARK R · 1994 to 2014
$4.1M
CORONAVIRUS--ANALYSIS OF POLYMERASE GENE PRODUCTSR29AI026603 · NIAID · VANDERBILT UNIVERSITY · PI DENISON, MARK R · 1988 to 1992
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NCI NIH HHS CA68485NCI NIH HHS P30 CA068485NHLBI NIH HHS T32 HL007751NHLBI NIH HHS T32 HL07751NIAID NIH HHS AI26603NIAID NIH HHS R01 AI026603
6 · The paper itself

Abstract

Despite ongoing research investigating mechanisms of coronavirus replication, functions of many viral nonstructural proteins (nsps) remain unknown. In the current study, a reverse genetic approach was used to define the role of the 28-kDa amino-terminal product (nsp1) of the gene 1 polyprotein during replication of the coronavirus murine hepatitis virus (MHV) in cell culture. To determine whether nsp1 is required for MHV replication and to identify residues critical for protein function, mutant viruses that contained deletions or point mutations within the nsp1-coding region were generated and assayed for defects in viral replication, viral protein expression, protein localization, and RNA synthesis. The results demonstrated that the carboxy-terminal half of nsp1 (residues K(124) through L(241)) was dispensable for virus replication in culture but was required for efficient proteolytic cleavage of nsp1 from the gene 1 polyprotein and for optimal viral replication. Furthermore, whereas deletion of nsp1 residues amino-terminal to K(124) failed to produce infectious virus, point mutagenesis of the nsp1 amino-terminus allowed recovery of several mutants with altered replication and RNA synthesis. This study identifies nsp1 residues important for protein processing, viral RNA synthesis, and viral replication.

Indexed as

Virus ReplicationAmino Acid SequenceAnimalsBase SequenceCell LineCricetinaeDNA PrimersKineticsMurine hepatitis virusMutagenesisPlasmidsReverse Transcriptase Polymerase Chain ReactionRNA, ViralViral Nonstructural ProteinsDNA PrimersNSP1 protein, murine hepatitis virusRNA, ViralViral Nonstructural Proteins

Identifiers

PMID16051301
PMCPMC7111834

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.